4fdg: Difference between revisions
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{{STRUCTURE_4fdg| PDB=4fdg | SCENE= }} | {{STRUCTURE_4fdg| PDB=4fdg | SCENE= }} | ||
===Crystal Structure of an Archaeal MCM Filament=== | |||
{{ABSTRACT_PUBMED_23361460}} | |||
== | ==Function== | ||
[[http://www.uniprot.org/uniprot/MCM_SULSO MCM_SULSO]] Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.<ref>PMID:11821426</ref> | |||
==About this Structure== | ==About this Structure== | ||
[[4fdg]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FDG OCA]. | [[4fdg]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FDG OCA]. | ||
==Reference== | |||
<references group="xtra"/><references/> | |||
[[Category: DNA helicase]] | [[Category: DNA helicase]] | ||
[[Category: Sulfolobus solfataricus]] | [[Category: Sulfolobus solfataricus]] | ||
Revision as of 07:56, 27 March 2013
Crystal Structure of an Archaeal MCM Filament
Template:ABSTRACT PUBMED 23361460
Function
[MCM_SULSO] Presumptive replicative helicase. Has ATPase and DNA helicase activities. The latter preferentially melts 5'-tailed oligonucleotides and is stimulated by the SSB protein (single-stranded DNA binding protein). The active ATPase sites in the MCM ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The helicase function is proposed to use a partially sequential mode of ATP hydrolysis; the complex appears to tolerate multiple catalytically inactive subunits.[1]
About this Structure
4fdg is a 5 chain structure with sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
- ↑ Carpentieri F, De Felice M, De Falco M, Rossi M, Pisani FM. Physical and functional interaction between the mini-chromosome maintenance-like DNA helicase and the single-stranded DNA binding protein from the crenarchaeon Sulfolobus solfataricus. J Biol Chem. 2002 Apr 5;277(14):12118-27. Epub 2002 Jan 30. PMID:11821426 doi:10.1074/jbc.M200091200
